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P55157

- MTP_HUMAN

UniProt

P55157 - MTP_HUMAN

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Protein

Microsomal triglyceride transfer protein large subunit

Gene
MTTP, MTP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the secretion of plasma lipoproteins that contain apolipoprotein B.

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. lipid transporter activity Source: Reactome

GO - Biological processi

  1. cholesterol homeostasis Source: Ensembl
  2. lipid metabolic process Source: ProtInc
  3. lipoprotein metabolic process Source: Reactome
  4. lipoprotein transport Source: Ensembl
  5. protein lipidation Source: Ensembl
  6. response to calcium ion Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. triglyceride metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_6841. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal triglyceride transfer protein large subunit
Gene namesi
Name:MTTP
Synonyms:MTP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:7467. MTTP.

Subcellular locationi

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. brush border membrane Source: Ensembl
  3. endoplasmic reticulum lumen Source: Reactome
  4. Golgi apparatus Source: Ensembl
  5. membrane-bounded vesicle Source: Ensembl
  6. microvillus membrane Source: Ensembl
  7. receptor complex Source: MGI
  8. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Abetalipoproteinemia (ABL) [MIM:200100]: An autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti540 – 5401R → H in ABL; loss of activity. 2 Publications
VAR_010642
Natural varianti590 – 5901S → I in ABL. 1 Publication
VAR_010643
Natural varianti746 – 7461G → E in ABL. 1 Publication
VAR_010644
Natural varianti780 – 7801N → Y in ABL; loss of activity. 1 Publication
VAR_014019

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi540 – 5401R → K: No change of activity. 1 Publication
Mutagenesisi878 – 8781C → S: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi200100. phenotype.
Orphaneti14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBiPA164742099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 894876Microsomal triglyceride transfer protein large subunitPRO_0000041593Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP55157.
PaxDbiP55157.
PRIDEiP55157.

PTM databases

PhosphoSiteiP55157.

Expressioni

Tissue specificityi

Liver and small intestine. Also found in ovary, testis and kidney.1 Publication

Inductioni

Positively regulated by cholesterol and negatively regulated by insulin.1 Publication

Gene expression databases

ArrayExpressiP55157.
BgeeiP55157.
CleanExiHS_MTTP.
GenevestigatoriP55157.

Organism-specific databases

HPAiHPA054862.

Interactioni

Subunit structurei

Heterodimer composed of MTTP and of protein disulfide isomerase (P4HB/PDI) By similarity.

Protein-protein interaction databases

BioGridi110641. 1 interaction.
MINTiMINT-1537333.
STRINGi9606.ENSP00000265517.

Structurei

3D structure databases

ProteinModelPortaliP55157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 659632VitellogeninAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG272516.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiP55157.
KOiK14463.
PhylomeDBiP55157.
TreeFamiTF328754.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view]
PfamiPF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55157-1 [UniParc]FASTAAdd to Basket

« Hide

MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK    50
LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNVE NVNQQRGEKS 100
IFKGKSPSKI MGKENLEALQ RPTLLHLIHG KVKEFYSYQN EAVAIENIKR 150
GLASLFQTQL SSGTTNEVDI SGNCKVTYQA HQDKVIKIKA LDSCKIARSG 200
FTTPNQVLGV SSKATSVTTY KIEDSFVIAV LAEETHNFGL NFLQTIKGKI 250
VSKQKLELKT TEAGPRLMSG KQAAAIIKAV DSKYTAIPIV GQVFQSHCKG 300
CPSLSELWRS TRKYLQPDNL SKAEAVRNFL AFIQHLRTAK KEEILQILKM 350
ENKEVLPQLV DAVTSAQTSD SLEAILDFLD FKSDSSIILQ ERFLYACGFA 400
SHPNEELLRA LISKFKGSIG SSDIRETVMI ITGTLVRKLC QNEGCKLKAV 450
VEAKKLILGG LEKAEKKEDT RMYLLALKNA LLPEGIPSLL KYAEAGEGPI 500
SHLATTALQR YDLPFITDEV KKTLNRIYHQ NRKVHEKTVR TAAAAIILNN 550
NPSYMDVKNI LLSIGELPQE MNKYMLAIVQ DILRFEMPAS KIVRRVLKEM 600
VAHNYDRFSR SGSSSAYTGY IERSPRSAST YSLDILYSGS GILRRSNLNI 650
FQYIGKAGLH GSQVVIEAQG LEALIAATPD EGEENLDSYA GMSAILFDVQ 700
LRPVTFFNGY SDLMSKMLSA SGDPISVVKG LILLIDHSQE LQLQSGLKAN 750
IEVQGGLAID ISGAMEFSLW YRESKTRVKN RVTVVITTDI TVDSSFVKAG 800
LETSTETEAG LEFISTVQFS QYPFLVCMQM DKDEAPFRQF EKKYERLSTG 850
RGYVSQKRKE SVLAGCEFPL HQENSEMCKV VFAPQPDSTS SGWF 894
Length:894
Mass (Da):99,351
Last modified:October 1, 1996 - v1
Checksum:iB20260C136BDAB9F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951Q → H.1 Publication
Corresponds to variant rs61733139 [ dbSNP | Ensembl ].
VAR_014016
Natural varianti98 – 981E → D.
Corresponds to variant rs2306986 [ dbSNP | Ensembl ].
VAR_052961
Natural varianti128 – 1281I → T.2 Publications
Corresponds to variant rs3816873 [ dbSNP | Ensembl ].
VAR_014017
Natural varianti166 – 1661N → S.
Corresponds to variant rs3792683 [ dbSNP | Ensembl ].
VAR_052962
Natural varianti168 – 1681V → I Rare polymorphism. 1 Publication
Corresponds to variant rs61750974 [ dbSNP | Ensembl ].
VAR_022658
Natural varianti244 – 2441Q → E.1 Publication
Corresponds to variant rs17599091 [ dbSNP | Ensembl ].
VAR_014018
Natural varianti297 – 2971H → Q.3 Publications
Corresponds to variant rs2306985 [ dbSNP | Ensembl ].
VAR_010640
Natural varianti354 – 3541E → Q.
Corresponds to variant rs12933 [ dbSNP | Ensembl ].
VAR_014916
Natural varianti384 – 3841D → A.1 Publication
Corresponds to variant rs17029215 [ dbSNP | Ensembl ].
VAR_010641
Natural varianti540 – 5401R → H in ABL; loss of activity. 2 Publications
VAR_010642
Natural varianti590 – 5901S → I in ABL. 1 Publication
VAR_010643
Natural varianti746 – 7461G → E in ABL. 1 Publication
VAR_010644
Natural varianti780 – 7801N → Y in ABL; loss of activity. 1 Publication
VAR_014019

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti585 – 5851F → L in CAA42200. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75500 mRNA. Translation: CAA53217.1.
X59657 mRNA. Translation: CAA42200.1.
X83013
, X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
AK290793 mRNA. Translation: BAF83482.1.
BC125110 mRNA. Translation: AAI25111.1.
BC125111 mRNA. Translation: AAI25112.1.
CCDSiCCDS3651.1.
PIRiI38047.
RefSeqiNP_000244.2. NM_000253.2.
UniGeneiHs.195799.

Genome annotation databases

EnsembliENST00000265517; ENSP00000265517; ENSG00000138823.
ENST00000457717; ENSP00000400821; ENSG00000138823.
GeneIDi4547.
KEGGihsa:4547.
UCSCiuc003hvc.4. human.

Polymorphism databases

DMDMi1709167.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75500 mRNA. Translation: CAA53217.1 .
X59657 mRNA. Translation: CAA42200.1 .
X83013
, X83014 , X83015 , X83016 , X83017 , X83018 , X83019 , X83020 , X83021 , X83022 , X83023 , X83024 , X83025 , X83026 , X83027 , X83028 , X83029 , X83030 Genomic DNA. Translation: CAA58142.1 .
AK290793 mRNA. Translation: BAF83482.1 .
BC125110 mRNA. Translation: AAI25111.1 .
BC125111 mRNA. Translation: AAI25112.1 .
CCDSi CCDS3651.1.
PIRi I38047.
RefSeqi NP_000244.2. NM_000253.2.
UniGenei Hs.195799.

3D structure databases

ProteinModelPortali P55157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110641. 1 interaction.
MINTi MINT-1537333.
STRINGi 9606.ENSP00000265517.

Chemistry

BindingDBi P55157.
ChEMBLi CHEMBL2569.
DrugBanki DB01094. Hesperetin.

PTM databases

PhosphoSitei P55157.

Polymorphism databases

DMDMi 1709167.

Proteomic databases

MaxQBi P55157.
PaxDbi P55157.
PRIDEi P55157.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265517 ; ENSP00000265517 ; ENSG00000138823 .
ENST00000457717 ; ENSP00000400821 ; ENSG00000138823 .
GeneIDi 4547.
KEGGi hsa:4547.
UCSCi uc003hvc.4. human.

Organism-specific databases

CTDi 4547.
GeneCardsi GC04P100485.
HGNCi HGNC:7467. MTTP.
HPAi HPA054862.
MIMi 157147. gene.
200100. phenotype.
neXtProti NX_P55157.
Orphaneti 14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBi PA164742099.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG272516.
HOGENOMi HOG000113688.
HOVERGENi HBG006416.
InParanoidi P55157.
KOi K14463.
PhylomeDBi P55157.
TreeFami TF328754.

Enzyme and pathway databases

Reactomei REACT_6841. Chylomicron-mediated lipid transport.

Miscellaneous databases

GeneWikii Microsomal_triglyceride_transfer_protein.
GenomeRNAii 4547.
NextBioi 17529.
PROi P55157.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55157.
Bgeei P55157.
CleanExi HS_MTTP.
Genevestigatori P55157.

Family and domain databases

Gene3Di 1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProi IPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view ]
Pfami PF01347. Vitellogenin_N. 1 hit.
[Graphical view ]
SMARTi SM00638. LPD_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEi PS51211. VITELLOGENIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein."
    Shoulders C.C., Brett D.J., Bayliss J.D., Narcisi T.M.E., Jarmuz A., Grantham T.T., Leoni P.R.D., Bhattacharya S., Pease R.J., Cullen P.M., Levi S., Byfield P.G.H., Purkiss P., Scott J.
    Hum. Mol. Genet. 2:2109-2116(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Small intestine.
  2. "Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia."
    Sharp D., Blinderman L., Combs K.A., Kienzle B., Ricci B., Wager-Smith K., Gil C.M., Turck C.W., Bouma M.-E., Rader D.J., Aggerbeck L.P., Gregg R.E., Gordon D.A., Wetterau J.R.
    Nature 365:65-69(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Human microsomal triglyceride transfer protein large subunit gene structure."
    Sharp D., Ricci B., Kienzle B., Lin M.C., Wetterau J.R.
    Biochemistry 33:9057-9061(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Transcriptional regulation of human and hamster microsomal triglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators."
    Hagan D.L., Kienzle B., Jamil H., Hariharan N.
    J. Biol. Chem. 269:28737-28744(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  7. "The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain."
    Shoulders C.C., Narcisi T.M.E., Read J., Chester S.A., Brett D.J., Scott J., Anderson T.A., Levitt D.G., Banaszak L.J.
    Nat. Struct. Biol. 1:285-286(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO VITELLOGENINS.
  8. "Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia."
    Narcisi T.M.E., Shoulders C.C., Chester S.A., Read J., Brett D.J., Harrison G.B., Grantham T.T., Fox M.F., Povey S., de Bruin T.W.A., Erkelens D.W., Muller D.P.R., Lloyd J.K., Scott J.
    Am. J. Hum. Genet. 57:1298-1310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-878.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase."
    Rehberg E.F., Samson-Bouma M.-E., Kienzle B., Blinderman L., Jamil H., Wetterau J.R., Aggerbeck L.P., Gordon D.A.
    J. Biol. Chem. 271:29945-29952(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL HIS-540, VARIANTS GLN-297 AND ALA-384, MUTAGENESIS OF ARG-540.
  11. "Microsomal triglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia."
    Wang J., Hegele R.A.
    Hum. Mutat. 15:294-295(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ABL HIS-540; ILE-590 AND GLU-746.
  12. "Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia."
    Ohashi K., Ishibashi S., Osuga J., Tozawa R., Harada K., Yahagi N., Shionoiri F., Iizuka Y., Tamura Y., Nagai R., Illingworth D.R., Gotoda T., Yamada N.
    J. Lipid Res. 41:1199-1204(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL TYR-780.
  13. "Variants of the microsomal triglyceride transfer protein gene are associated with plasma cholesterol levels and body mass index."
    Ledmyr H., Karpe F., Lundahl B., McKinnon M., Skoglund-Andersson C., Ehrenborg E.
    J. Lipid Res. 43:51-58(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-95; THR-128; GLU-244 AND GLN-297.
  14. "Hypobetalipoproteinemia with an apparently recessive inheritance due to a 'de novo' mutation of apolipoprotein B."
    Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., Bertolini S., Calandra S., Tarugi P.
    Biochim. Biophys. Acta 1688:61-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-128; ILE-168 AND GLN-297.

Entry informationi

Entry nameiMTP_HUMAN
AccessioniPrimary (citable) accession number: P55157
Secondary accession number(s): A8K428, Q08AM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi